Histidine transaminase
| Histidine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.38 | ||||||||
| CAS no. | 37277-92-2 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Histidine transaminase (EC 2.6.1.38) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme characterised from Escherichia coli and Pseudomonas acidovorans are L-histidine and α-ketoglutaric acid. Its products are imidazole-4-pyruvic acid and L-glutamic acid.[1][2]
This enzyme is a transferase, specifically a transaminase, which transfer nitrogenous groups. The systematic name of this enzyme class is L-histidine:2-oxoglutarate aminotransferase. Other names in common use include histidine aminotransferase, and histidine-2-oxoglutarate aminotransferase. It participates in histidine metabolism.[3]
References
- ↑ Wickremasinghe R, Hedegaard J, Roche J (1967). "Degradation de la L-histidine chez Escherichia coli B: formation de l'acide imidazolepyruvique par une histidine-transaminase". C. R. Soc. Biol. 161: 1891–1896.
- ↑ Coote JG, Hassall H (1969). "The role of imidazol-5-yl-lactate-nicotinamide-adenine dinucleotide phosphate oxidoreductase and histidine-2-oxoglutarate aminotransferase in the degradation of imidazol-5-yl-lactate by Pseudomonas acidovorans". Biochem. J. 111 (2): 237–9. doi:10.1042/bj1110237. PMC 1187811. PMID 4303364.
- ↑ Enzyme 2.6.1.38 at KEGG Pathway Database.
Categories: